B0FWC7 (COX1_AEDAE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 35.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cytochrome c oxidase subunit 1 EC=1.9.3.1 Alternative name(s): Cytochrome c oxidase polypeptide I | ||||
| Gene names |
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| Encoded on | Mitochondrion | ||||
| Organism | Aedes aegypti (Yellowfever mosquito) (Culex aegypti) [Reference proteome] | ||||
| Taxonomic identifier | 7159 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Culicinae › Aedini › Aedes › Stegomyia![]() |
Protein attributes
| Sequence length | 514 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. |
| Catalytic activity | 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O. |
| Pathway | |
| Subcellular location | |
| Sequence similarities | Belongs to the heme-copper respiratory oxidase family. |
| Sequence caution | The sequence ABY51624.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 514 | 514 | Cytochrome c oxidase subunit 1 | PRO_0000347262 | |||||||
Regions | |||||||||||
| Transmembrane | 16 – 36 | 21 | Helical; Potential | ||||||||
| Transmembrane | 55 – 75 | 21 | Helical; Potential | ||||||||
| Transmembrane | 101 – 117 | 17 | Helical; Potential | ||||||||
| Transmembrane | 144 – 164 | 21 | Helical; Potential | ||||||||
| Transmembrane | 182 – 202 | 21 | Helical; Potential | ||||||||
| Transmembrane | 233 – 253 | 21 | Helical; Potential | ||||||||
| Transmembrane | 267 – 287 | 21 | Helical; Potential | ||||||||
| Transmembrane | 304 – 324 | 21 | Helical; Potential | ||||||||
| Transmembrane | 337 – 357 | 21 | Helical; Potential | ||||||||
| Transmembrane | 379 – 399 | 21 | Helical; Potential | ||||||||
| Transmembrane | 415 – 435 | 21 | Helical; Potential | ||||||||
| Transmembrane | 451 – 471 | 21 | Helical; Potential | ||||||||
Sites | |||||||||||
| Metal binding | 60 | 1 | Iron (heme A axial ligand) By similarity UniProtKB P98002 | ||||||||
| Metal binding | 239 | 1 | Copper B By similarity UniProtKB P98002 | ||||||||
| Metal binding | 243 | 1 | Copper B By similarity UniProtKB P98002 | ||||||||
| Metal binding | 289 | 1 | Copper B By similarity UniProtKB P98002 | ||||||||
| Metal binding | 290 | 1 | Copper B By similarity UniProtKB P98002 | ||||||||
| Metal binding | 375 | 1 | Iron (heme A3 axial ligand) By similarity UniProtKB P98002 | ||||||||
| Metal binding | 377 | 1 | Iron (heme A axial ligand) By similarity UniProtKB P98002 | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 239 ↔ 243 | 1'-histidyl-3'-tyrosine (His-Tyr) By similarity UniProtKB P98002 | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 171 | 1 | R → W in ABY51624. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The mitochondrial genome of the Yellow fever mosquito - Aedes aegypti." Lobo N.F., Lovin D., DeBruyn B., Puiu D., Shumway M., Haas B., Nene V., Severson D.W. Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LVPib12. |
| [2] | "Complete mitochondrial DNA sequence and amino acid analysis of the cytochrome C oxidase subunit I (COI) from Aedes aegypti." Morlais I., Severson D.W. DNA Seq. 13:123-127(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 2-513. Strain: Formosus, Liverpool, Moyo-R and Red eye. Tissue: Midgut. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | EU352212 Genomic DNA. Translation: ABY51624.1. Sequence problems. AF380835 Genomic DNA. Translation: AAK56378.2. AF390098 mRNA. Translation: AAK73349.2. AY056596 Genomic DNA. Translation: AAL25639.1. AY056597 Genomic DNA. Translation: AAL25640.1. |
| RefSeq | YP_001649163.1. NC_010241.1. |
3D structure databases | |
| ProteinModelPortal | B0FWC7. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 5848241. |
| KEGG | aag:COX1. |
Organism-specific databases | |
| CTD | 4512. |
Phylogenomic databases | |
| KO | K02256. |
| ProtClustDB | MTH00153. |
Enzyme and pathway databases | |
| UniPathway | UPA00705. |
Family and domain databases | |
| Gene3D | 1.20.210.10. 1 hit. |
| InterPro | IPR000883. Cyt_c_Oxase_su1. IPR023615. Cyt_c_Oxase_su1_BS. IPR023616. Cyt_c_Oxase_su1_dom. [Graphical view] |
| PANTHER | PTHR10422. PTHR10422. 1 hit. |
| Pfam | PF00115. COX1. 1 hit. [Graphical view] |
| PRINTS | PR01165. CYCOXIDASEI. |
| SUPFAM | SSF81442. COX1. 1 hit. |
| PROSITE | PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | COX1_AEDAE | ||||||||
| Accession | Primary (citable) accession number: B0FWC7 Secondary accession number(s): Q94PR3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
